The molecular mechanism by which the membrane protein bacteriorhodopsin uses light energy to pump protons from the intracellular fluid into the extracellular space against an electrochemical gradient has been under serious study for many years. The chromophore, retinal, isomerizes about double bonds in its polyene chain as a consequence of altered torsion potentials in the electronic states to which it is excited by light absorption. Under investigation is how these chromophore isomerizations lead to net proton translocation. Based on previous studies, we are attempting to ascertain if the 1H T1 is indeed short at low temperature (30K) which would indicate the feasability of low temperature solid-state NMR studies via cross polarization. The enhanced Boltzman population at this temperature would permit experiments that have hitherto been unrealistic on account of marginal signal to noise ratios. An initial application that is serving as a feasability test is the investigation of oriented bR signal lineshapes of residues near the chromophore-protein linkage.